Assembling a program in bioinorganic chemistry that is scientifi cally relevant, well defined, and self-consistent is not an easy task. In this attempt we decided to consider zinc enzymes, copper oxidases, cytochromes and cytochrome oxidase. The choice is in part due to the great attention that the current specialized literature devotes to these topics, which are now debated among chemists, biochemists, biophysicists, etc .. We believe that hydration reactions, hydrolytic and oxidative processes have much in common from the point of view of the reaction mechanisms, the comprehension of which…mehr
Assembling a program in bioinorganic chemistry that is scientifi cally relevant, well defined, and self-consistent is not an easy task. In this attempt we decided to consider zinc enzymes, copper oxidases, cytochromes and cytochrome oxidase. The choice is in part due to the great attention that the current specialized literature devotes to these topics, which are now debated among chemists, biochemists, biophysicists, etc .. We believe that hydration reactions, hydrolytic and oxidative processes have much in common from the point of view of the reaction mechanisms, the comprehension of which represents a frontier of science. For these reasons these topics have been the subject of the NATO-ASI held at San Miniato, Pisa, Italy, from May 28 to June 8, 1982. We hope we can transfer here the main conclusions of what (we believe) was a very stimulating scientific meeting. We would like to thank the local saving bank, Cassa di Risparmio di San Miniato, for helping in many ways. The financial contribution from the European Research Office of the US Army, and from the Bruker Spectrospin s.r.l., Italy, is also acknowledged. The National Science Foundation of the United States has provided a travel grant to one of the participants from the U.S.A. We are grateful to the NATO Scientific Affairs Division which provided a grant to finance this Institute.Hinweis: Dieser Artikel kann nur an eine deutsche Lieferadresse ausgeliefert werden.
I: The Coordination Properties of the Active Site of Zinc Enzymes.- 1. Introduction.- 2. The Residues Coordinated at the Zinc Ion.- 3. The Acid-Base Properties of Coordinated Water.- 4. The Electronic Spectra of Cobalt (II) Derivatives.- 5. The Water 1H NMR Studies.- 6. The Implications on the Catalytic Mechanism.- II: Coordinated Solvent Molecules in Metalloenzymes and Proteins Studied Using NMRD.- 1. Introduction.- 2. The "Fluoromet" Mechanism.- 3. Fe3+ - Transferrin.- 4. Cu2+ - and V02+ - Transferrin.- 5. Co2+ - Carbonic Anhydrase.- 6. Alcohol Dehydrogenase.- 7. Mn2+ - Carboxypeptidase A.- 8. Conclusions.- III: 113Cd Nuclear Magnetic Resonance Studies of Zinc Metalloproteins.- 1. Introduction.- 2. Chemical Shifts.- 3. Sensitivity.- 4. Information Content.- 5. Concluding Remarks.- IV: Carbonic Anhydrase: Structure, Kinetics, and Mechanism.- 1. Introduction.- 2. Structure.- 3. Kinetics.- 4. Mechanism.- V: Metal Ion Promoted Hydrolysis of Nucleoside 5'-Triphosphates.- 1. Introduction.- 2. Results and Discussion.- VI: Models of Metalloenzymes: Carboxypeptidase A.- 1. Introduction.- 2. Metal Ion Catalyzed Hydrolysis of Amides and Esters.- 3. Results and Discussion.- 4. Cu2+ Mediated Amide Hydrolysis.- 5. Conclusions.- VII: Spectroscopic Studies on Cobalt(II) Carboxypeptidase A.- VIII: Coordination Properties and Mechanistic Aspects of Liver Alcohol Dehydrogenase.- 1. Introduction.- 2. Coordination Chemistry of Metallo Alcohol Dehydrogenases.- 3. Mechanistic Aspects.- IX: Metal-Directed Affinity Labelling and Promoted Alkylation of a Thiol Liganded to the Catalytic Metal Ion in Liver Alcohol Dehydrogenase.- 1. Introduction.- 2. Experimental.- 3. Results and Discussion.- X: Ligand Sphere Transitions: A New Concept in Zinc-Enzyme Catalysis.- 1. Introduction.-2. Experimental Background.- 3. The Proposed Model Concept.- XI: Molecular Mechamisms of the Superoxide Dismutase Activity of the Cuprozinc Protein of Eucaryotic Cells (CuZn Superoxide Dismutase).- 1. Molecular Properties of the Protein.- 2. General Mechanism of the Superoxide Dismutation by the Copper of the Protein.- 3. Inactivation of the Enzyme.- 4. Inhibition of the Enzyme.- 5. Role of the Zinc.- XII: A Comment on Anion Binding to Superoxide Dismutase.- XIII: Kinetic and Magnetic Resonance Studies on Amine Oxidases.- 1. Introduction.- 2. Studies on the Copper Cofactor.- 3. Mechanistic Studies.- XIV: Metal Coordination and Mechanism of Blue Copper Containing Oxidases.- 1. Introduction.- 2. Chemical Composition and Reactions Catalyzed.- 3. Spectroscopic Data.- 4. Oxidation-Reduction Properties.- 5. The Catalytic Mechanism.- XV: Metal Replacement Studies of Chinese Laccase.- 1. Introduction.- 2. Metal-Replacement Studies of Small Blue Proteins.- 3. The Removal and Replacement of Copper from Chinese Laccase.- 4. The Preparation of a Mixed-Metal Hybrid of Laccase.- XVI: Reactions of Rhus Vernicifera Laccase with Azide and Fluoride, Formation of a "Half-Met-N3 -Type" Binding.- 1. Reactions with N3- as Studied by EPR.- 2. Reactions with N3- in the Presence of Redox Reagents.- 3. Half-Met-N3-Type Binding in Laccase.- 4. Reactions with Fluoride.- 5. Temperature Effects.- XVII: Structural Magnetic Correlations in Exchange Coupled Systems.- 1. Spin Hamiltonian Approach to Exchange Coupling.- 2. Molecular Orbital Approach to Exchange Coupling.- XVIII: Structural and Magnetic Investigations on Model CU4O4 Cubane-Like Clusters.- 1. Introduction.- 2. Structural Description.- 3. Magnetic Properties and Structural Data.- 4. Extension of the Correlations Between Magnetism andStructures.- 5. Example.- XIX: Neurospora Tyrosinase: Intrinsic and Extrinsic Fluorescence.- 1. Introduction.- 2. Intrinsic Fluorescence.- 3. Extrinsic Fluorescence.- XX: Comparison of Two Fungal Tyrosinases.- 1. Introduction.- 2. Molecular Properties.- 3. Properties of the Copper Site.- 4. Identification of Endogenous Ligands.- 5. Inhibition by Anions.- XXI: Activation of Molecular Oxygen.- 1. Introduction.- 2. Autoxidation Reactions.- 3. Wacker Oxidations.- 4. Oxidations by Metal Bound 02.- 5. Oxidations by Products Derived from Metal-O2 Species.- 6. Oxygen Atom Transfer Reactions.- 7. Conclusion.- XXII: Mössbauer Studies on Putidamonooxin - A New Type of [2Fe-2S] Containing Oxygenase Component with a Mononuclear Non-Heme Iron Ion as Cofactor.- 1. Introduction.- 2. Mössbauer Spectroscopic Investigation.- 3. Conclusion.- XXIII: The Enzyme-Substrate Interaction in the Catechol Dioxygenases.- XXIV: Ferric Nitrilotriacetate: An Active Center Analogue of Pyrocatechase.- XXV: Stereoselective Peroxidatic Activity of Iron(III) Complex Ions Supported on Polypeptides.- XXVI: NMR Studies of Cytochromes.- 1. Introduction.- 2. Class II Cytochromes c.- 3. Low Spin Cytochromes.- 4. Electron Transfer Mechanisms.- XXVII: The Structure of the Metal Centers in Cytochrome c Oxidase.- 1. Introduction.- 2. The Metal Centers.- 3. Summary.- XXVIII: Models of Metalloenzymes: Peroxidase and Cytochrome P-450.- 1. Introduction.- 2. Model Systems.- XXIX: Coordination Chemistry of Cytochrome P-450 and Herne Models.- 1. Introduction: Occurrence and Function of Cytochrome P450-Dependent Monooxygenases.- 2. The Catalytic Cycle of Cytochrome P450.- 3. Cytochrome P450-Iron Comlexes Formed by Direct Interaction with Organic Compounds.- 4. Cytochrome P450-Iron-Metabolite Complexes.- 5. Conclusion:The Unique Richness of Cytochrome P450 Coordination Chemistry.- XXX: Mössbauer Studies of Synthetic Analogues for the Active Site in Cytochromes P450.- 1. Introduction.- 2. Preparation of the Compounds.- 3. X-ray Structures.- 4. Mössbauer Studies.- 5. Molecular Orbital Calculations and ?EQ- Interpretation.- XXXI: Magnetic Circular Dichroism Spectroscopy as a Probe of Ferric Cytochrome P-450 and its Ligand Complexes.- 1. Introduction.- 2. Materials and Methods.- 3. Results and Discussion.- 4. Conclusion.
I: The Coordination Properties of the Active Site of Zinc Enzymes.- 1. Introduction.- 2. The Residues Coordinated at the Zinc Ion.- 3. The Acid-Base Properties of Coordinated Water.- 4. The Electronic Spectra of Cobalt (II) Derivatives.- 5. The Water 1H NMR Studies.- 6. The Implications on the Catalytic Mechanism.- II: Coordinated Solvent Molecules in Metalloenzymes and Proteins Studied Using NMRD.- 1. Introduction.- 2. The "Fluoromet" Mechanism.- 3. Fe3+ - Transferrin.- 4. Cu2+ - and V02+ - Transferrin.- 5. Co2+ - Carbonic Anhydrase.- 6. Alcohol Dehydrogenase.- 7. Mn2+ - Carboxypeptidase A.- 8. Conclusions.- III: 113Cd Nuclear Magnetic Resonance Studies of Zinc Metalloproteins.- 1. Introduction.- 2. Chemical Shifts.- 3. Sensitivity.- 4. Information Content.- 5. Concluding Remarks.- IV: Carbonic Anhydrase: Structure, Kinetics, and Mechanism.- 1. Introduction.- 2. Structure.- 3. Kinetics.- 4. Mechanism.- V: Metal Ion Promoted Hydrolysis of Nucleoside 5'-Triphosphates.- 1. Introduction.- 2. Results and Discussion.- VI: Models of Metalloenzymes: Carboxypeptidase A.- 1. Introduction.- 2. Metal Ion Catalyzed Hydrolysis of Amides and Esters.- 3. Results and Discussion.- 4. Cu2+ Mediated Amide Hydrolysis.- 5. Conclusions.- VII: Spectroscopic Studies on Cobalt(II) Carboxypeptidase A.- VIII: Coordination Properties and Mechanistic Aspects of Liver Alcohol Dehydrogenase.- 1. Introduction.- 2. Coordination Chemistry of Metallo Alcohol Dehydrogenases.- 3. Mechanistic Aspects.- IX: Metal-Directed Affinity Labelling and Promoted Alkylation of a Thiol Liganded to the Catalytic Metal Ion in Liver Alcohol Dehydrogenase.- 1. Introduction.- 2. Experimental.- 3. Results and Discussion.- X: Ligand Sphere Transitions: A New Concept in Zinc-Enzyme Catalysis.- 1. Introduction.-2. Experimental Background.- 3. The Proposed Model Concept.- XI: Molecular Mechamisms of the Superoxide Dismutase Activity of the Cuprozinc Protein of Eucaryotic Cells (CuZn Superoxide Dismutase).- 1. Molecular Properties of the Protein.- 2. General Mechanism of the Superoxide Dismutation by the Copper of the Protein.- 3. Inactivation of the Enzyme.- 4. Inhibition of the Enzyme.- 5. Role of the Zinc.- XII: A Comment on Anion Binding to Superoxide Dismutase.- XIII: Kinetic and Magnetic Resonance Studies on Amine Oxidases.- 1. Introduction.- 2. Studies on the Copper Cofactor.- 3. Mechanistic Studies.- XIV: Metal Coordination and Mechanism of Blue Copper Containing Oxidases.- 1. Introduction.- 2. Chemical Composition and Reactions Catalyzed.- 3. Spectroscopic Data.- 4. Oxidation-Reduction Properties.- 5. The Catalytic Mechanism.- XV: Metal Replacement Studies of Chinese Laccase.- 1. Introduction.- 2. Metal-Replacement Studies of Small Blue Proteins.- 3. The Removal and Replacement of Copper from Chinese Laccase.- 4. The Preparation of a Mixed-Metal Hybrid of Laccase.- XVI: Reactions of Rhus Vernicifera Laccase with Azide and Fluoride, Formation of a "Half-Met-N3 -Type" Binding.- 1. Reactions with N3- as Studied by EPR.- 2. Reactions with N3- in the Presence of Redox Reagents.- 3. Half-Met-N3-Type Binding in Laccase.- 4. Reactions with Fluoride.- 5. Temperature Effects.- XVII: Structural Magnetic Correlations in Exchange Coupled Systems.- 1. Spin Hamiltonian Approach to Exchange Coupling.- 2. Molecular Orbital Approach to Exchange Coupling.- XVIII: Structural and Magnetic Investigations on Model CU4O4 Cubane-Like Clusters.- 1. Introduction.- 2. Structural Description.- 3. Magnetic Properties and Structural Data.- 4. Extension of the Correlations Between Magnetism andStructures.- 5. Example.- XIX: Neurospora Tyrosinase: Intrinsic and Extrinsic Fluorescence.- 1. Introduction.- 2. Intrinsic Fluorescence.- 3. Extrinsic Fluorescence.- XX: Comparison of Two Fungal Tyrosinases.- 1. Introduction.- 2. Molecular Properties.- 3. Properties of the Copper Site.- 4. Identification of Endogenous Ligands.- 5. Inhibition by Anions.- XXI: Activation of Molecular Oxygen.- 1. Introduction.- 2. Autoxidation Reactions.- 3. Wacker Oxidations.- 4. Oxidations by Metal Bound 02.- 5. Oxidations by Products Derived from Metal-O2 Species.- 6. Oxygen Atom Transfer Reactions.- 7. Conclusion.- XXII: Mössbauer Studies on Putidamonooxin - A New Type of [2Fe-2S] Containing Oxygenase Component with a Mononuclear Non-Heme Iron Ion as Cofactor.- 1. Introduction.- 2. Mössbauer Spectroscopic Investigation.- 3. Conclusion.- XXIII: The Enzyme-Substrate Interaction in the Catechol Dioxygenases.- XXIV: Ferric Nitrilotriacetate: An Active Center Analogue of Pyrocatechase.- XXV: Stereoselective Peroxidatic Activity of Iron(III) Complex Ions Supported on Polypeptides.- XXVI: NMR Studies of Cytochromes.- 1. Introduction.- 2. Class II Cytochromes c.- 3. Low Spin Cytochromes.- 4. Electron Transfer Mechanisms.- XXVII: The Structure of the Metal Centers in Cytochrome c Oxidase.- 1. Introduction.- 2. The Metal Centers.- 3. Summary.- XXVIII: Models of Metalloenzymes: Peroxidase and Cytochrome P-450.- 1. Introduction.- 2. Model Systems.- XXIX: Coordination Chemistry of Cytochrome P-450 and Herne Models.- 1. Introduction: Occurrence and Function of Cytochrome P450-Dependent Monooxygenases.- 2. The Catalytic Cycle of Cytochrome P450.- 3. Cytochrome P450-Iron Comlexes Formed by Direct Interaction with Organic Compounds.- 4. Cytochrome P450-Iron-Metabolite Complexes.- 5. Conclusion:The Unique Richness of Cytochrome P450 Coordination Chemistry.- XXX: Mössbauer Studies of Synthetic Analogues for the Active Site in Cytochromes P450.- 1. Introduction.- 2. Preparation of the Compounds.- 3. X-ray Structures.- 4. Mössbauer Studies.- 5. Molecular Orbital Calculations and ?EQ- Interpretation.- XXXI: Magnetic Circular Dichroism Spectroscopy as a Probe of Ferric Cytochrome P-450 and its Ligand Complexes.- 1. Introduction.- 2. Materials and Methods.- 3. Results and Discussion.- 4. Conclusion.
Es gelten unsere Allgemeinen Geschäftsbedingungen: www.buecher.de/agb
Impressum
www.buecher.de ist ein Internetauftritt der buecher.de internetstores GmbH
Geschäftsführung: Monica Sawhney | Roland Kölbl | Günter Hilger
Sitz der Gesellschaft: Batheyer Straße 115 - 117, 58099 Hagen
Postanschrift: Bürgermeister-Wegele-Str. 12, 86167 Augsburg
Amtsgericht Hagen HRB 13257
Steuernummer: 321/5800/1497
USt-IdNr: DE450055826
